In the past year, the relationship of pyridoxine status in the pyridoxine deficient rat to the activities of the glucocorticoid-receptor complexes has been measured. When the receptor from deficient animals is studied in vitro, there is a pronounced increase in the rate and extent of activation and binding to DNA-cellulose or to normal nuclei. When the hormone is injected into pyridoxine deficient rats, there is a marked reduction in intrahepatocyte content of (3H)triamcinolone acetonide compared to deficient pyridoxine-supplemented controls. These experiments lead us to conclude that the translocation process is more efficient in vivo in pyridoxine deficiency and allow the conclusion that this vitamin is involved in the overall regulation of the glucocorticoid receptor.